Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-08-15 |
Detector | ADSC CCD |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 59.292, 62.064, 74.893 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 18.470 - 1.000 |
R-factor | 0.1 |
Rwork | 0.100 |
R-free | 0.11000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1uqx |
RMSD bond length | 0.022 |
RMSD bond angle | 1.977 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0003) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 18.600 | 1.010 |
High resolution limit [Å] | 1.000 | 1.000 |
Rmerge | 0.060 | 0.390 |
Number of reflections | 73738 | |
<I/σ(I)> | 14.68 | 2.65 |
Completeness [%] | 99.0 | 97.3 |
Redundancy | 2.92 | 2.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8.2 | 5UL DROPS OF 10MG/ML PROTEIN DISSOLVED IN WATER MIXED WITH 5UL DROPS OF 8% PEG 10000, 0.1M TRIS HCL, PH 8.2 WITH MANNOSE AT 270UG/ML |